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Database: UniProt
Entry: A0A091DKJ1_FUKDA
LinkDB: A0A091DKJ1_FUKDA
Original site: A0A091DKJ1_FUKDA 
ID   A0A091DKJ1_FUKDA        Unreviewed;      1204 AA.
AC   A0A091DKJ1;
DT   26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT   26-NOV-2014, sequence version 1.
DT   24-JAN-2024, entry version 40.
DE   RecName: Full=RING-type E3 ubiquitin transferase {ECO:0000256|ARBA:ARBA00012483};
DE            EC=2.3.2.27 {ECO:0000256|ARBA:ARBA00012483};
GN   ORFNames=H920_07883 {ECO:0000313|EMBL:KFO30780.1};
OS   Fukomys damarensis (Damaraland mole rat) (Cryptomys damarensis).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Hystricomorpha; Bathyergidae;
OC   Fukomys.
OX   NCBI_TaxID=885580 {ECO:0000313|EMBL:KFO30780.1, ECO:0000313|Proteomes:UP000028990};
RN   [1] {ECO:0000313|EMBL:KFO30780.1, ECO:0000313|Proteomes:UP000028990}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   TISSUE=Liver {ECO:0000313|EMBL:KFO30780.1};
RA   Gladyshev V.N., Fang X.;
RT   "The Damaraland mole rat (Fukomys damarensis) genome and evolution of
RT   African mole rats.";
RL   Submitted (NOV-2013) to the EMBL/GenBank/DDBJ databases.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=S-ubiquitinyl-[E2 ubiquitin-conjugating enzyme]-L-cysteine +
CC         [acceptor protein]-L-lysine = [E2 ubiquitin-conjugating enzyme]-L-
CC         cysteine + N(6)-ubiquitinyl-[acceptor protein]-L-lysine.;
CC         EC=2.3.2.27; Evidence={ECO:0000256|ARBA:ARBA00000900};
CC   -!- PATHWAY: Protein modification; protein ubiquitination.
CC       {ECO:0000256|ARBA:ARBA00004906}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
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DR   EMBL; KN122382; KFO30780.1; -; Genomic_DNA.
DR   RefSeq; XP_010628458.1; XM_010630156.1.
DR   AlphaFoldDB; A0A091DKJ1; -.
DR   STRING; 885580.ENSFDAP00000006083; -.
DR   GeneID; 104866269; -.
DR   CTD; 9666; -.
DR   eggNOG; KOG0800; Eukaryota.
DR   OrthoDB; 5256194at2759; -.
DR   UniPathway; UPA00143; -.
DR   Proteomes; UP000028990; Unassembled WGS sequence.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0003723; F:RNA binding; IEA:InterPro.
DR   GO; GO:0061630; F:ubiquitin protein ligase activity; IEA:InterPro.
DR   GO; GO:0000209; P:protein polyubiquitination; IEA:InterPro.
DR   CDD; cd16460; RING-H2_DZIP3; 1.
DR   Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 1.
DR   InterPro; IPR033103; DZIP3_RING-H2_finger.
DR   InterPro; IPR041249; HEPN_DZIP3.
DR   InterPro; IPR043866; TTC3/DZIP3_dom.
DR   InterPro; IPR001841; Znf_RING.
DR   InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR   PANTHER; PTHR15727:SF4; E3 UBIQUITIN-PROTEIN LIGASE DZIP3; 1.
DR   PANTHER; PTHR15727; RING FINGER PROTEIN 214; 1.
DR   Pfam; PF18738; HEPN_DZIP3; 1.
DR   Pfam; PF19179; TTC3_DZIP3_dom; 1.
DR   Pfam; PF13639; zf-RING_2; 1.
DR   SMART; SM00184; RING; 1.
DR   SUPFAM; SSF57850; RING/U-box; 1.
DR   PROSITE; PS50089; ZF_RING_2; 1.
PE   4: Predicted;
KW   Coiled coil {ECO:0000256|SAM:Coils};
KW   Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Reference proteome {ECO:0000313|Proteomes:UP000028990};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833};
KW   Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW   ProRule:PRU00175}.
FT   DOMAIN          1144..1184
FT                   /note="RING-type"
FT                   /evidence="ECO:0000259|PROSITE:PS50089"
FT   REGION          1..40
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          636..713
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1085..1135
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          776..849
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COMPBIAS        1..16
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        25..40
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        669..691
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1085..1131
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1204 AA;  137847 MW;  6F438CCFDE793949 CRC64;
     MDSLPEEFFV REAAVEDQNE EETENEVEKS AIQPDKQKKD IPTDLVPGDL LLEVKKLLNA
     INTLPKGVVP HIKKFLQEDF CFQTMQREVA ASSQNGEEVV PALTLRFLIT QLETALRNIQ
     ATNYTAYQID IGYYLTLLFL YGVSLTERGK KEDYTEAENK FLVMKMVIQE NEICENFMSL
     VYFGRGLLRC AQKRYNGGLL EFHKSLQEIG DINDHWFDID PTEDEDLPTN FKDLLNSFIK
     TTENNIMKQT ICSYLDCERS CEADILKNTN YKGFFQLMCS KNCCIYFHKI CWKKFKNLKY
     PGENDQSFSG KTCLKEGCTG DMVRMLQGDV PGTVKILFEV VRKDECITIE NLGASYKKLM
     SLKIADTDIR PKIGLKFNTK DEMPIFKLDY NYFYHLLHII IISGTDIVRQ IFDEAMPPPL
     LKKELLIHKN VLESYYNHLW TNHPLGGSWH LLYPPNKELP QSKQFDLCLL LALIKHLNVF
     PAPQKGWIME PPSSDLSKSA DILRLCKYRD ILLSEILMNG LTESQFNSIW KKVSDILLRL
     GMKQEDIDKV KENPIENISL DYHQLSIYLG IPVPEIIQRM LSCYQQGIAL QSITGSQRIE
     IEELQNEEED LSPPLMEYNI NVKSNSELQL ADMNKDGASI PSESSTESVK DLQEVKSKPK
     KKKTTKHKKS KDSKEEKISY MREKEEQLKN EQTNPHPMGR FMKDDAGDQE DSATEDKFYS
     LDELHILDMI EQGSTGKVTT DCGETEKERL VQQQLYKLHY RCEDFKKQLK TMIFRCQENQ
     MQIKKKEKII ASLNQQVTFG INKVSKLQRQ VHAKDNEIKN FKEQFSMKRS QWEMEKHNLE
     STIKTYLNKL NAETSRALTA EVYFLQCRRD FGLLHLEQTE KECLSQLARV THMAASSLES
     LQLKAAVDSW NSIVADVRNK IAVLRTQYNE QINKVKQGFP LSSLPPIQLP PPPPSPELLM
     QQYLGRPIVK DSFFRPILTV PQMPAICPAV ISAPGQPRPP LMTGIAWTMP TPVGETVPPS
     AGLGTDLSLM NWERITDRLK TAFPQQTRKE LTDFLLKLKE AHGKSLSGLT CDEIVYKISQ
     FIDPKKPQSQ EKTVPNGNVS PSDSSSQTNA PQPPKSAWSS LSSQGSATWE EANNVDEEEE
     EEPCVICHEN LSPENLSVLP CAHKFHSQCI RPWLMQQGTC PTCRLHVLLP EEFPGHTSQQ
     LPKV
//
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